OST48_DICDI
ID OST48_DICDI Reviewed; 426 AA.
AC Q54E62;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit;
DE Short=DDOST 48 kDa subunit;
DE Short=Oligosaccharyl transferase 48 kDa subunit;
DE Flags: Precursor;
GN Name=ddost; Synonyms=ost48; ORFNames=DDB_G0291780;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. {ECO:0000250|UniProtKB:P33767}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P33767}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000184; EAL61549.1; -; Genomic_DNA.
DR RefSeq; XP_629963.1; XM_629961.1.
DR AlphaFoldDB; Q54E62; -.
DR SMR; Q54E62; -.
DR STRING; 44689.DDB0233148; -.
DR PaxDb; Q54E62; -.
DR PRIDE; Q54E62; -.
DR EnsemblProtists; EAL61549; EAL61549; DDB_G0291780.
DR GeneID; 8628330; -.
DR KEGG; ddi:DDB_G0291780; -.
DR dictyBase; DDB_G0291780; wbp1.
DR eggNOG; KOG2754; Eukaryota.
DR HOGENOM; CLU_031804_0_0_1; -.
DR InParanoid; Q54E62; -.
DR OMA; YQFKVDY; -.
DR PhylomeDB; Q54E62; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q54E62; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:dictyBase.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..426
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase 48 kDa subunit"
FT /id="PRO_0000328637"
FT TOPO_DOM 23..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 426 AA; 47889 MW; C14040D8C68810C7 CRC64;
MMMKSILITF IIASALLSSV FADIGGKRTL VVLDDLSIKK THSTFFKNLE NKGYKLQFEQ
SNTKVVLEKY GDFNFDNLIL FSPTSESLSF SSADVTRFID GGNNVLFAGS NVISENIRDI
AAECGMEIEE DKTLIFDHFN YDKSQSDHSV LVADQFIDDS PIILQGLNKP ILFKGIGHKI
RNNPLNYAIL TGSSTAFSAK AISGVSTKLM GKSCGLVSSL QARNNARVTF SGSLDLFSDK
SFYSKIDNKE SGNKEFVERL VSWTFQERGI LRASELELVK ISTESNSTVA PDVFTIKDEV
KYSLKVEEFD GIKGKWVPYV GSLQLEVIML DPYIRTFIKG DANGLYKIHF KLPDVYGVFT
FEASIHKSGY STLDHIYRKP ILPFRHDSYE RFIPAAFPYY ATCFSMLIGT FIFSIIFLFN
KDQLNK
